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Published June 1, 1978 | public
Journal Article Open

Pseudomonas Cytochrome c551 at 2.0 angstrom Resolution: Enlargement of the Cytochrome c Family


The structure of respiratory cytochrome c551 of Pseudomonas aeruginosa, with 82 amino acids, has been solved by x-ray analysis and refined to a crystallographic R factor of 16.2%. It has the same basic folding pattern and hydrophobic heme environment as cytochromes c, c2, and c550, except for a large deletion at the bottom of the heme crevice. This same "cytochrome fold" appears to be present in photosynthetic cytochromes c of green and purple sulfur bacteria, and algal cytochromes f, suggesting a common evolutionary origin for electron transport chains in photosynthesis and respiration.

Additional Information

Copyright © 1978 by the National Academy of Sciences. Communicated by John D. Baldeschwieler, March 20, 1978. We thank Dr. Richard P. Ambler for permission to mention unpublished results prior to publication. This investigation was supported by the National Institutes of Health under Grant GM-12121 and the National Science Foundation under Grant PCM75-05586. This is contribution no. 5632 of the Norman W. Church Laboratory of Chemical Biology. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.


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